2b83

A single amino acid substitution in the Clostridium beijerinckii alcohol dehydrogenase is critical for thermostabilization
(see also Tetrameric alcohol dehydrogenases)



The crystal structure of Clostridium beijerinckii alcohol dehydrogenase (CbADH; EC 1.1.1.2) with the substitution Q100P (tetramer ) was solved at 2.25 Å resolution. The substitution of Gln100 with Pro did not cause significant structural changes in the protein structure. The residues of the wildtype protein are colored lime and the residues of the mutant one in cyan. Only 2 H-bonds were lost, one between Oε1 of Gln100 and the main chain N of Gly297, and the second between Nε2 of Gln100 and the main chain carbonyl O of Gly297. The mutation caused that an additional CH2 group (Cδ of Pro100) is surrounded by nonpolar residues: Pro88 (3.8 Å), Trp90 (3.5 Å), and Val95 (4 Å). These residues (P100, P88, W90, and V95) are situated on a protruding lobe of the protein. An additional 11 aliphatic and aromatic carbon atoms are situated within the distance of 6 Å from Cδ of Pro100 (two methyl groups of Val95; three carbon atoms of the Trp90 indole group; Cβ and Cγ methylene groups of Pro100; Cβ and Cγ of Gln101, and two carbons of the Phe99 phenyl ring).

About this Structure
2B83 is a Single protein structure of sequence from Clostridium beijerinckii. Full crystallographic information is available from OCA.

Reference
A single proline substitution is critical for the thermostabilization of Clostridium beijerinckii alcohol dehydrogenase., Goihberg E, Dym O, Tel-Or S, Levin I, Peretz M, Burstein Y, Proteins. 2007 Jan 1;66(1):196-204. PMID:17063493

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